1887

Abstract

SUMMARY: Increasing doses of alkylating agents such as -methyl--nitro--nitrosoguanidine, diethyl sulphate and ethylmethane sulphonate cause an inhibition of the expression of the and genes of wild-type This behaviour was not observed in a mutant which has a defective LexA repressor that is unable to bind to the SOS operator. Furthermore, an mutant showed the same behaviour as the wild-type strain indicating that the adaptive proteins are not responsible for the inhibition of and at high doses of alkylating agents. These results suggest that the inhibitory effect of these alkylating agents may be found in the interaction between the LexA repressor and the control regions of and On the other hand, high doses of either UV light or mitomycin C produced only a slight decrease in the induction of and , whereas bleomycin had no effect. The fact that a repressor structurally related to LexA repressor, such as LacI protein, showed the same behaviour as the LexA repressor when a Lac strain was treated with alkylating agents, suggests that these compounds can modify the binding abilities of repressors to DNA, producing a limited or even abolished release of repressors, and so decreasing the expression of inducible genes.

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1986-10-01
2022-01-20
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References

  1. Anderson W. F., Takeda Y., Ohlendorf D. H., Matthews B. W. 1982; Proposed α-helical super-secondary structure associated with protein–DNA recognition. Journal of Molecular Biology 159:745–751
    [Google Scholar]
  2. Auerbach C. 1976; In Mutation Research: Problems, Results, and Perspectives. pp 504–553 London: Chapman & Hall;
    [Google Scholar]
  3. Barbé J., Vericat J. A., Guerrero R. 1983; Discriminated induction of SOS functions in Escherichia coli by alkylating agents. Journal of General Microbiology 129:2079–2089
    [Google Scholar]
  4. Barbé, J., Cairó J., Vericat J. A., Guerrero R. 1985; Further characterization of SOS system in recBC mutants of Escherichia coli. Mutation Research 146:23–32
    [Google Scholar]
  5. Clark D. J., Maaløe O. 1967; DNA replication and the division cycle of Escherichia coli. Journal of Molecular Biology 23:99–112
    [Google Scholar]
  6. Crooke S. T. 1981; Mitomycin C; an overview. In Cancer and Chemotherapy vol. 3 pp. 49–60 Edited by Crooke S. T., Prestayco A. W. New York: Academic Press;
    [Google Scholar]
  7. D’Andrea A. D., Haseltine W. A. 1978; Sequence specific cleavage of DNA by the antitumor antibiotics neocarzinostatin and bleomycin. Proceedings of the National Academy of Sciences of the United States of America 75:3608–3612
    [Google Scholar]
  8. Guerrero R., Barbé J. 1982; Expression of recA-gene dependent SOS functions in Salmonella typhimurium. Antonie van Leeuwenhoek 48:159–167
    [Google Scholar]
  9. Helène C. 1977; Specific recognition of guanine bases in protein–nucleic acid complexes. FEBS Letters 74:10–13
    [Google Scholar]
  10. Hoffmann G. R. 1980; Genetic effects of dimethyl sulfate, diethyl sulfate and related compounds. Mutation Research 75:63–129
    [Google Scholar]
  11. Jeggo P., Defais M., Samson L., Schendel P. 1977; An adaptive response of E. coli to low levels of alkylating agents: comparison with previously characterized DNA repair pathways. Molecular and General Genetics 157:1–9
    [Google Scholar]
  12. Kenyon C. J., Walker G. C. 1981; Expression of the E. coli uvrA gene is inducible. Nature, London 289:808–810
    [Google Scholar]
  13. Kunkel G. R., Martinson H. G. 1978; Histone–DNA interactions within chromatin. Isolation of histones from DNA–histone adducts induced in nuclei by UV light. Nucleic Acids Research 5:4263–4272
    [Google Scholar]
  14. Lawley P. D. 1974; Some chemical aspects of dose-response relationships in alkylating mutagenesis. Mutation Research 23:283–295
    [Google Scholar]
  15. Lawley P. D., Orr D. J. 1970; Specific excision of methylation products from DNA of Escherichia coli treated with N-methyl-N′-nitro-N-nitrosoguanidine. Chemico-Biological Interactions 2:154–157
    [Google Scholar]
  16. Lin S.-Y., Riggs A. D. 1972; Lac operator analogues: bromodeoxyuridine substitution in the lac operator affects the rate of dissociation of the lac repressor. Proceedings of the National Academy of Sciences of the United States of America 69:2574–2576
    [Google Scholar]
  17. Lin S.-Y., Riggs A. D. 1976; The binding of lac repressor and the catabolite gene activator protein to halogen-substituted analogues of poly [d(A-T)]. Biochimica et biophysica acta 432:185–191
    [Google Scholar]
  18. Little J. W., Mount D. W. 1982; The SOS regulatory system of Escherichia coli. Cell 29:11–22
    [Google Scholar]
  19. Little J. W., Edmiston S. M., Pacelli L. Z., Mount D. W. 1980; Cleavage of the Escherichia coli LexA protein by the RecA protease. Proceedings of the National Academy of Sciences of the United States of America 77:3225–3229
    [Google Scholar]
  20. Markovitz A. 1972; Ultraviolet light-induced stable complexes on DNA and DNA polymerase. Biochimica et biophysica acta 281:522–534
    [Google Scholar]
  21. Matthews B. W., Ohlendorf D. H., Anderson W. F., Fisher R. G., Takeda Y. 1983; Cro repressor protein and its interaction with DNA. Cold Spring Harbor Symposia on Quantitative Biology 47:427–433
    [Google Scholar]
  22. Miller J. M. 1972; Experiments in Molecular Genetics. Cold Spring Harbor New York: Cold Spring Harbor Laboratories;
    [Google Scholar]
  23. Moreau P. L., Fanica M., Devoret R. 1980; Induction of prophage lambda does not require full induction of recA protein synthesis. Biochimie 62:687–694
    [Google Scholar]
  24. Ohta T., Nakamura N., Moriya M., Shirasu Y., Kada T. 1984; The SOS-function-inducing activity of chemical mutagens in Escherichia coli. Mutation Research 131:101–109
    [Google Scholar]
  25. Oishi M., Smith C. L., Friefeld B. 1979; Molecular events and molecules that lead to induction of prophage and SOS functions. Cold Spring Harbor Symposia on Quantitative Biology 43:897–907
    [Google Scholar]
  26. Pabo C. O., Lewis M. 1982; The operator-binding domain of λ repressor: structure and DNA recognition. Nature, London 298:441–443
    [Google Scholar]
  27. Pabo C. O., Krovatin W., Jeffrey A., Sauer R. T. 1982; The N-terminal arms of λ repressor wrap around the operator DNA. Nature, London 298:444–446
    [Google Scholar]
  28. Roberts J. W., Roberts C. W., Craig N. L. 1978; Escherichia coli recA gene product inactivates phage λ repressor. Proceedings of the National Academy of Sciences of the United States of America 75:4714–4718
    [Google Scholar]
  29. Sauer R. T., Pabo C. O., Meyer B. J., Ptashne M., Backman K. C. 1979; Regulatory functions of the λ repressor reside in the amino-terminal domain. Nature, London 279:396–400
    [Google Scholar]
  30. Sauer R. T., Yocum R. R., Doolittle R. F., Lewis M., Pabo C. O. 1982a; Homology among DNA-binding proteins suggest use of a conserved super-secondary structure. Nature, London 298:447–451
    [Google Scholar]
  31. Sauer R. T., Ross M. J., Ptashne M. 1982b; Cleavage of the λ and P22 repressors by recA protein. Journal of Biological Chemistry 257:4458–4462
    [Google Scholar]
  32. Schendel P. F., Fogliano M., Strausbaugh L. D. 1982; Regulation of the Escherichia coli K12 uvrB operon. Journal of Bacteriology 150:676–685
    [Google Scholar]
  33. Simic M. G., Dizdaroglu M. 1985; Formation of radiation-induced cross-links between thymine and tyrosine: possible model for cross-linking of DNA and proteins by ionizing radiation. Biochemistry 24:233–236
    [Google Scholar]
  34. Smith T. F., Sadler J. R. 1971; The nature of lactose operator constitutive mutants. Journal of Molecular Biology 59:273–305
    [Google Scholar]
  35. Smith C. L., Siegfried E., Ruvolo P. P. 1983; Adaptive doses of MNNG induce a recA-trp gene fusion. DNA 2:291–299
    [Google Scholar]
  36. Steitz T. A., Weber I. T., Mathew J. B. 1983; Catabolite gene activator protein: structure, homology with other proteins, and cyclic AMP and DNA binding. Cold Spring Harbor Symposia on Quantitative Biology 47:419–426
    [Google Scholar]
  37. Vericat J. A., Barbé J., Guerrero R. 1984; Expression of the SOS response following simultaneous treatment with methyl-nitrosoguanidine and mitomycin C in Escherichia coli. Mutation Research 132:15–20
    [Google Scholar]
  38. Walker G. C. 1984; Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli. Microbiological Reviews 48:60–93
    [Google Scholar]
  39. Witkin E. M. 1974; Thermal enhancement of ultraviolet mutability in a tif uvrA derivative of Escherichia coli B/r: evidence that ultraviolet mutagenesis depends on an inducible function. Proceedings of the National Academy of Sciences of the United States of America 71:1930–1934
    [Google Scholar]
  40. Yoda K., Sakiyama S., Fujimura S. 1982; Interaction of N-ethyl-N′-nitro-N-nitrosoguanidine with nucleic acids and proteins in comparison with N-methyl-N′-nitro-N-nitrosoguanidine. Chemico-Biological Interactions 41:49–59
    [Google Scholar]
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